YYL performed the laboratory work, including the mutant construct

YYL performed the laboratory work, including the mutant construction and complementation, gene expression, and time-kill assays. HWL carried out the MIC determinations. CYL participated in the overall design of this study and assisted in writing the manuscript. All authors have read and approved the final manuscript.”
“Background PXD101 solubility dmso peroxidases (EC 1.11.1.x) are a group of oxidoreductases that catalyse the oxidation of various compounds by using peroxides. While hydrogen peroxide (H2O2) is commonly used as an electron donor, peroxidases can take a variety of different

substrates as electron acceptors. Peroxidases can be divided into two major groups, contingent upon the presence selleck chemicals or absence of a haem cofactor. Among their numerous industrial applications, one good example would be their ability to remove phenolic compounds from wastewater, NVP-BSK805 mw in which haem peroxidases are involved. For instance, peroxidases including horseradish peroxidase enzymatically catalyse the conversion of phenolic substrates into phenoxy radicals. The resulted phenoxy radicals can chemically react among themselves or with other substrates, consequently causing precipitation of polymeric products, which can be easily separated from the wastewater [1, 2]. In addition, lignin peroxidase

(LiP) and manganese peroxidase (MnP) are considered to be the most effective enzymes for recycling carbon sources fixed as lignin [3]. As genes encoding LiP are quite limited to white rot fungi, including Phanerochaete chrysosporium[4, 5], P. sordida[6], Trametes versicolor[7], Phlebia radiata[8, 9], P. tremellosa[10],

and Bjerkandera sp. [11], genes encoding MnP have drawn attention as an alternative ligninolytic peroxidase due to their wider distribution among basidiomycetes Acyl CoA dehydrogenase compared to those encoding LiP. Furthermore, site-directed mutagenesis on LiP and MnP genes revealed that the catalytic residues play pivotal roles in switching enzymatic activities between LiP and MnP in P. chrysosporium[12, 13]. Recently, a new type of haem protein called versatile peroxidases (VPs) has been found in Pleurotus and Bjerkandera species that can naturally perform both functions [14, 15]. Hence, they are considered to be another candidates for ligninolysis. Meanwhile, a dye-decolorizing peroxidase (DyP), MsP1, in Marasmius scorodonius is thought to be useful for industrial applications due to its high temperature and pressure stability [16]. Besides their industrial impacts, peroxidases are also important in fungal pathogenicity on host animals and plants. For example, deletion mutants of a gene encoding thiol peroxidase, TSA1, in Cryptococcus neoformans showed significantly less virulence on mice [17]. For plant pathogens, peroxidases are required to detoxify host-driven reactive oxygen species for Ustilago maydis[18] and Magnaporthe oryzae[19].

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